Search

Your search keyword '"Chao-Sheng Chen"' showing total 4 results
Start Over Author "Chao-Sheng Chen" Publisher the royal society
4 results on '"Chao-Sheng Chen"'

1. Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response

Author

Natacha Larburu, Christopher J. Adams, Chao-Sheng Chen, Piotr R. Nowak, and Maruf M. U. Ali

Subjects
hsp70 chaperones, protein translocation, upr, bip, ire1, tim44, Biology (General), QH301-705.5
Abstract

Hsp70 chaperones interact with substrate proteins in a coordinated fashion that is regulated by nucleotides and enhanced by assisting cochaperones. There are numerous homologues and isoforms of Hsp70 that participate in a wide variety of cellular functions. This diversity can facilitate adaption or specialization based on particular biological activity and location within the cell. In this review, we highlight two specialized binding partner proteins, Tim44 and IRE1, that interact with Hsp70 at the membrane in order to serve their respective roles in protein translocation and unfolded protein response signalling. Recent mechanistic data suggest analogy in the way the two Hsp70 homologues (BiP and mtHsp70) can bind and release from IRE1 and Tim44 upon substrate engagement. These shared mechanistic features may underlie how Hsp70 interacts with specialized binding partners and may extend our understanding of the mechanistic repertoire that Hsp70 chaperones possess.

Published
2020
Full Text
View/download PDF

3. Mechanism of Hsp70 specialised interactions in protein translocation and the unfolded protein response

Author

Maruf M.U. Ali, Piotr Nowak, Natacha Larburu, Christopher J. Adams, Chao-Sheng Chen, and Cancer Research UK

Subjects
Gene isoform, Models, Molecular, BiP, Immunology, Review, Review Article, IRE1, UPR, Biology, Endoplasmic Reticulum, 0601 Biochemistry and Cell Biology, General Biochemistry, Genetics and Molecular Biology, Substrate Specificity, Structure-Activity Relationship, Animals, Humans, Nucleotide, HSP70 Heat-Shock Proteins, Protein translocation, lcsh:QH301-705.5, chemistry.chemical_classification, protein translocation, Mechanism (biology), General Neuroscience, Cell Membrane, Hsp70 chaperones, Hsp70, Cell biology, Mitochondria, Tim44, Protein Transport, lcsh:Biology (General), chemistry, Gene Expression Regulation, 1107 Immunology, Unfolded protein response, Unfolded Protein Response, Carrier Proteins, Molecular Chaperones, Protein Binding, 0605 Microbiology
Abstract

Hsp70 chaperones interact with substrate proteins in a coordinated fashion that is regulated by nucleotides and enhanced by assisting cochaperones. There are numerous homologues and isoforms of Hsp70 that participate in a wide variety of cellular functions. This diversity can facilitate adaption or specialization based on particular biological activity and location within the cell. In this review, we highlight two specialized binding partner proteins, Tim44 and IRE1, that interact with Hsp70 at the membrane in order to serve their respective roles in protein translocation and unfolded protein response signalling. Recent mechanistic data suggest analogy in the way the two Hsp70 homologues (BiP and mtHsp70) can bind and release from IRE1 and Tim44 upon substrate engagement. These shared mechanistic features may underlie how Hsp70 interacts with specialized binding partners and may extend our understanding of the mechanistic repertoire that Hsp70 chaperones possess.

Published
2020

Catalog

Books, media, physical & digital resources
See catalog results